GLP1_BRANA
ID GLP1_BRANA Reviewed; 207 AA.
AC P46271;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Germin-like protein 1;
DE Flags: Precursor;
GN Name=GER1;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samourai; TISSUE=Seedling;
RX PubMed=9349269; DOI=10.1023/a:1005833028582;
RA Membre N., Berna A., Neutelings G., David A., David H., Staiger D.,
RA Saez Vasquez J., Raynal M., Delseny M., Bernier F.;
RT "cDNA sequence, genomic organization and differential expression of three
RT Arabidopsis genes for germin/oxalate oxidase-like proteins.";
RL Plant Mol. Biol. 35:459-469(1997).
CC -!- FUNCTION: May play a role in plant defense. Probably has no oxalate
CC oxidase activity even if the active site is conserved.
CC -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR EMBL; U21743; AAA86365.1; -; mRNA.
DR PIR; T07854; T07854.
DR RefSeq; NP_001302724.1; NM_001315795.1.
DR AlphaFoldDB; P46271; -.
DR SMR; P46271; -.
DR GeneID; 106354228; -.
DR KEGG; bna:106354228; -.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR001929; Germin.
DR InterPro; IPR019780; Germin_Mn-BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 1.
DR PRINTS; PR00325; GERMIN.
DR SMART; SM00835; Cupin_1; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00725; GERMIN; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Disulfide bond; Glycoprotein; Manganese; Metal-binding; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..207
FT /note="Germin-like protein 1"
FT /id="PRO_0000010836"
FT DOMAIN 51..197
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..38
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 21514 MW; B6A29465A73B956E CRC64;
MLRIIFLLSL LFALSNDSVQ DFCVANLKRA ETPAGYPCIR PIHVKASDFV FSLGTPGNTT
NIISAAVTPG FVAQFPALNG LGISTARLDL APKGVIPMHT HPGASEVLFV LDGSITAGFI
SSANSVYVQT LKPGQVMVFP QGLLHFQINA GKTPAAALVT FSSASPGLQI LDFALFANTL
STELVSATTF LPPATVKTLK GVLGGTG